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Shinichi Kohsaka - One of the best experts on this subject based on the ideXlab platform.
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direct interaction of post Synaptic Density 95 dlg zo 1 domain containing Synaptic molecule shank3 with glur1 alpha amino 3 hydroxy 5 methyl 4 isoxazole propionic acid receptor
Journal of Neurochemistry, 2006Co-Authors: Shigeo Uchino, Hidenori Wada, Shizuyo Honda, Yasuko Nakamura, Yumiko Ondo, Takayoshi Uchiyama, Moe Tsutsumi, Eri Suzuki, Takae Hirasawa, Shinichi KohsakaAbstract:A class of scaffolding protein containing the post-Synaptic Density-95/Dlg/ZO-1 (PDZ) domain is thought to be involved in Synaptic trafficking of α-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid (AMPA) receptors during development. To clarify the molecular mechanism of AMPA receptor trafficking, we performed a yeast two-hybrid screening system using the cytoplasmic tail of the GluR1 subunit of AMPA receptor as a bait and identified a Synaptic molecule, Shank3/ProSAP2, as a GluR1 subunit-interacting molecule. Shank3 is a PDZ domain-containing multidomain protein and is predominantly expressed in developing neurons. Using the glutathione S-transferase pull-down assay and immunoprecipitation technique we demonstrated that the GluR1 subunit directly binds to the PDZ domain of Shank3 via its carboxyl terminal PDZ-binding motif. We raised anti-Shank3 antibody to investigate the expression of Shank3 in cortical neurons. The pattern of Shank3 immunoreactivity was strikingly punctate, mainly observed in the spines, and closely matched the pattern of post-Synaptic Density-95 immunoreactivity, indicating that Shank3 is colocalized with post-Synaptic Density-95 in the same spines. When Shank3 and the GluR1 subunit were overexpressed in primary cortical neurons, they were also colocalized in the spines. Taken together with the biochemical interaction of Shank3 with the GluR1 subunit, these results suggest that Shank3 is an important molecule that interacts with GluR1 AMPA receptor at Synaptic sites of developing neurons.
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Direct interaction of post-Synaptic Density-95/Dlg/ZO-1 domain-containing Synaptic molecule Shank3 with GluR1 alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptor.
Journal of neurochemistry, 2006Co-Authors: Shigeo Uchino, Hidenori Wada, Shizuyo Honda, Yasuko Nakamura, Yumiko Ondo, Takayoshi Uchiyama, Moe Tsutsumi, Eri Suzuki, Takae Hirasawa, Shinichi KohsakaAbstract:A class of scaffolding protein containing the post-Synaptic Density-95/Dlg/ZO-1 (PDZ) domain is thought to be involved in Synaptic trafficking of α-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid (AMPA) receptors during development. To clarify the molecular mechanism of AMPA receptor trafficking, we performed a yeast two-hybrid screening system using the cytoplasmic tail of the GluR1 subunit of AMPA receptor as a bait and identified a Synaptic molecule, Shank3/ProSAP2, as a GluR1 subunit-interacting molecule. Shank3 is a PDZ domain-containing multidomain protein and is predominantly expressed in developing neurons. Using the glutathione S-transferase pull-down assay and immunoprecipitation technique we demonstrated that the GluR1 subunit directly binds to the PDZ domain of Shank3 via its carboxyl terminal PDZ-binding motif. We raised anti-Shank3 antibody to investigate the expression of Shank3 in cortical neurons. The pattern of Shank3 immunoreactivity was strikingly punctate, mainly observed in the spines, and closely matched the pattern of post-Synaptic Density-95 immunoreactivity, indicating that Shank3 is colocalized with post-Synaptic Density-95 in the same spines. When Shank3 and the GluR1 subunit were overexpressed in primary cortical neurons, they were also colocalized in the spines. Taken together with the biochemical interaction of Shank3 with the GluR1 subunit, these results suggest that Shank3 is an important molecule that interacts with GluR1 AMPA receptor at Synaptic sites of developing neurons.
Andreas W. Püschel - One of the best experts on this subject based on the ideXlab platform.
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semaphorin 4b interacts with the post Synaptic Density protein psd 95 sap90 and is recruited to synapses through a c terminal pdz binding motif
FEBS Letters, 2005Co-Authors: Constanze Burkhardt, Myriam Müller, Anja Badde, Craig C. Garner, Eckart D. Gundelfinger, Andreas W. PüschelAbstract:The semaphorins are a large family of proteins that act as guidance signals for axons and dendrites. The class 4 semaphorins are integral membrane proteins that are widely expressed throughout the nervous system. Here, we show that a subclass of these semaphorins is characterized by a PDZ-binding motif at their carboxy-terminus. This sequence mediates the interaction with the post-Synaptic Density protein PSD-95/SAP90. Co-expression of Sema4B with PSD-95 in COS 7 cells results in the clustering of Sema4B. Sema4B co-localizes with PSD-95 at Synaptic contacts between cultured hippocampal neurons. This Synaptic localization depends on the presence of the PDZ-binding motif.
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Semaphorin 4B interacts with the post-Synaptic Density protein PSD-95/SAP90 and is recruited to synapses through a C-terminal PDZ-binding motif.
FEBS letters, 2005Co-Authors: Constanze Burkhardt, Myriam Müller, Anja Badde, Craig C. Garner, Eckart D. Gundelfinger, Andreas W. PüschelAbstract:The semaphorins are a large family of proteins that act as guidance signals for axons and dendrites. The class 4 semaphorins are integral membrane proteins that are widely expressed throughout the nervous system. Here, we show that a subclass of these semaphorins is characterized by a PDZ-binding motif at their carboxy-terminus. This sequence mediates the interaction with the post-Synaptic Density protein PSD-95/SAP90. Co-expression of Sema4B with PSD-95 in COS 7 cells results in the clustering of Sema4B. Sema4B co-localizes with PSD-95 at Synaptic contacts between cultured hippocampal neurons. This Synaptic localization depends on the presence of the PDZ-binding motif.
Chiahsiang Chen - One of the best experts on this subject based on the ideXlab platform.
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genetic and functional analysis of the dlg4 gene encoding the post Synaptic Density protein 95 in schizophrenia
PLOS ONE, 2010Co-Authors: Minchih Cheng, Syueng Luu, Homin Tsai, Shihhsin Hsu, Tzuting Chen, Chiahsiang ChenAbstract:Hypofunction of N-methyl-D-aspartate (NMDA) receptor-mediated signal transduction has been implicated in the pathophysiology of schizophrenia. Post-Synaptic Density protein 95 (PSD95) plays a critical role in regulating the trafficking and activity of the NMDA receptor and altered expression of the PSD95 has been detected in the post-mortem brain of patients with schizophrenia. The study aimed to examine whether the DLG4 gene that encodes the PSD95 may confer genetic susceptibility to schizophrenia. We re-sequenced the core promoter, all the exons, and 3′ untranslated regions (UTR) of the DLG4 gene in 588 Taiwanese schizophrenic patients and conducted an association study with 539 non-psychotic subjects. We did not detect any rare mutations at the protein-coding sequences of the DLG4 gene associated with schizophrenia. Nevertheless, we identified four polymorphic markers at the core promoter and 5′ UTR and one single nucleotide polymorphism (SNP) at the 3′UTR of the DLG4 gene in this sample. Genetic analysis showed an association of a haplotype (C–D) derived from 2 polymorphic markers at the core promoter (odds ratio = 1.26, 95% confidence interval = 1.06–1.51, p = 0.01), and a borderline association of the T allele of the rs13331 at 3′UTR with schizophrenia (odds ratio = 1.19, 95% confidence interval = 0.99–1.43, p = 0.06). Further reporter gene assay showed that the C-D-C-C and the T allele of the rs13331 had significant lower activity than their counter parts. Our data indicate that the expression of the DLG4 gene is subject to regulation by the polymorphic markers at the core promoter region, 5′ and 3′UTR of the gene, and is associated with the susceptibility of schizophrenia.
S W Bolden - One of the best experts on this subject based on the ideXlab platform.
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Structural asymmetry in the thalamofugal visual projections in 2-day-old chick is correlated with a hemispheric difference in Synaptic Density in the hyperstriatum accessorium.
Brain research, 1992Co-Authors: M G Stewart, L J Rogers, H A Davies, S W BoldenAbstract:Differences in visual discrimination ability between the left and right eyes of chicks, which are most prominent in young males, may result from a structural asymmetry in the organization of the visual projections from the thalamus to the visual Wulst. This asymmetry in projections is no longer present by 21 days in males when the contralateral projections from the right thalamus to the left hyperstriatum have developed. Since the asymmetry of the thalamo-hyperstriatal system results in a differential input of fibres to regions of the hyperstriatum which in turn project to the hyperstriatum accessorium (HA), one of the major differences expected within this region would be an asymmetry in the numerical Density of synapses (Nv.syn/microns3). When this was examined in the hyperstriatum accessorium of 2-day-old male chicks, the Density of synapses in the right HA was found to be significantly higher (22%, P less than 0.05) than in the left HA. The consequences of this asymmetry in Synaptic Density in the HA could be widespread and influential within the chick visual system.
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Structural asymmetry in the thalamofugal visual projections in 2-day-old chick is correlated with a hemispheric difference in Synaptic Density in the hyperstriatum accessorium.
Brain Research, 1992Co-Authors: Michael G. Stewart, Heather A. Davies, L J Rogers, S W BoldenAbstract:Differences in visual discrimination ability between the left and right eyes of chicks, which are most prominent in young males, may result from a structural asymmetry in the organization of the visual projections from the thalamus to the visual Wulst. This asymmetry in projections is no longer present by 21 days in males when the contralateral projections from the right thalamus to the left hyperstriatum have developed. Since the asymmetry of the thalamo-hyperstriatal system results in a differential input of fibres to regions of the hyperstriatum which in turn project to the hyperstriatum accessorium (HA), one of the major differences expected within this region would be an asymmetry in the numerical Density of synapses (Nv,syn/μm3). When this was examined in the hyperstriatum of 2-day-old male chicks, the Density of synapses in the right HA was found to be significantly higher (22%, P < 0.05) than in the left HA. The consequences of this asymmetry in Synaptic Density in the HA could be widespread and influential within the chick visual system.
Shigeo Uchino - One of the best experts on this subject based on the ideXlab platform.
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direct interaction of post Synaptic Density 95 dlg zo 1 domain containing Synaptic molecule shank3 with glur1 alpha amino 3 hydroxy 5 methyl 4 isoxazole propionic acid receptor
Journal of Neurochemistry, 2006Co-Authors: Shigeo Uchino, Hidenori Wada, Shizuyo Honda, Yasuko Nakamura, Yumiko Ondo, Takayoshi Uchiyama, Moe Tsutsumi, Eri Suzuki, Takae Hirasawa, Shinichi KohsakaAbstract:A class of scaffolding protein containing the post-Synaptic Density-95/Dlg/ZO-1 (PDZ) domain is thought to be involved in Synaptic trafficking of α-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid (AMPA) receptors during development. To clarify the molecular mechanism of AMPA receptor trafficking, we performed a yeast two-hybrid screening system using the cytoplasmic tail of the GluR1 subunit of AMPA receptor as a bait and identified a Synaptic molecule, Shank3/ProSAP2, as a GluR1 subunit-interacting molecule. Shank3 is a PDZ domain-containing multidomain protein and is predominantly expressed in developing neurons. Using the glutathione S-transferase pull-down assay and immunoprecipitation technique we demonstrated that the GluR1 subunit directly binds to the PDZ domain of Shank3 via its carboxyl terminal PDZ-binding motif. We raised anti-Shank3 antibody to investigate the expression of Shank3 in cortical neurons. The pattern of Shank3 immunoreactivity was strikingly punctate, mainly observed in the spines, and closely matched the pattern of post-Synaptic Density-95 immunoreactivity, indicating that Shank3 is colocalized with post-Synaptic Density-95 in the same spines. When Shank3 and the GluR1 subunit were overexpressed in primary cortical neurons, they were also colocalized in the spines. Taken together with the biochemical interaction of Shank3 with the GluR1 subunit, these results suggest that Shank3 is an important molecule that interacts with GluR1 AMPA receptor at Synaptic sites of developing neurons.
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Direct interaction of post-Synaptic Density-95/Dlg/ZO-1 domain-containing Synaptic molecule Shank3 with GluR1 alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptor.
Journal of neurochemistry, 2006Co-Authors: Shigeo Uchino, Hidenori Wada, Shizuyo Honda, Yasuko Nakamura, Yumiko Ondo, Takayoshi Uchiyama, Moe Tsutsumi, Eri Suzuki, Takae Hirasawa, Shinichi KohsakaAbstract:A class of scaffolding protein containing the post-Synaptic Density-95/Dlg/ZO-1 (PDZ) domain is thought to be involved in Synaptic trafficking of α-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid (AMPA) receptors during development. To clarify the molecular mechanism of AMPA receptor trafficking, we performed a yeast two-hybrid screening system using the cytoplasmic tail of the GluR1 subunit of AMPA receptor as a bait and identified a Synaptic molecule, Shank3/ProSAP2, as a GluR1 subunit-interacting molecule. Shank3 is a PDZ domain-containing multidomain protein and is predominantly expressed in developing neurons. Using the glutathione S-transferase pull-down assay and immunoprecipitation technique we demonstrated that the GluR1 subunit directly binds to the PDZ domain of Shank3 via its carboxyl terminal PDZ-binding motif. We raised anti-Shank3 antibody to investigate the expression of Shank3 in cortical neurons. The pattern of Shank3 immunoreactivity was strikingly punctate, mainly observed in the spines, and closely matched the pattern of post-Synaptic Density-95 immunoreactivity, indicating that Shank3 is colocalized with post-Synaptic Density-95 in the same spines. When Shank3 and the GluR1 subunit were overexpressed in primary cortical neurons, they were also colocalized in the spines. Taken together with the biochemical interaction of Shank3 with the GluR1 subunit, these results suggest that Shank3 is an important molecule that interacts with GluR1 AMPA receptor at Synaptic sites of developing neurons.
